122242-30-2

Upstream product

• 405-39-0 N,N'-di-[(phenylmethoxy)carbonyl]-L-lysine 
• 14316-06-4 D-alanine methyl ester hydrochloride 
• 120335-48-0 N-(N²,N⁶-bis-benzyloxycarbonyl-L-lysyl)-L-alanine ethyl ester 
• 120744-88-9 N-(N²,N⁶-bis-benzyloxycarbonyl-L-lysyl)-D-alanine ethyl ester 
• 1378999-76-8 C₂₆H₃₃N₃O₇ 

Downstream Products

• 16806-35-2 Lys-D-Ala-OH 
• 24570-39-6 (R)-2-[(R)-2-((S)-2,6-Bis-acetylamino-hexanoylamino)-propionylamino]-propionic acid 
• 16806-35-2 (S)-2-((S)-2,6-Diamino-hexanoylamino)-propionic acid 

Relevant academic research and scientific papers

Structure diversification of vancomycin through peptide-catalyzed, site-selective lipidation: A catalysis-based approach to combat glycopeptide-resistant pathogens

The emergence of antibiotic-resistant infections highlights the need for novel antibiotic leads, perhaps with a broader spectrum of activity. Herein, we disclose a semisynthetic, catalytic approach for structure diversification of vancomycin. We have identified three unique peptide catalysts that exhibit site-selectivity for the lipidation of the aliphatic hydroxyls on vancomycin, generating three new derivatives 9a, 9b, and 9c. Incorporation of lipid chains into the vancomycin scaffold provides promising improvement of its bioactivity against vancomycin-resistant enterococci (Van A and Van B phenotypes of VRE). The MICs for 9a, 9b, and 9c against MRSA and VRE (Van B phenotype) range from 0.12 to 0.25 μg/mL. We have also performed a structure-activity relationship (SAR) study to investigate the effect of lipid chain length at the newly accessible G4-OH derivatization site.

Catalytic site-selective thiocarbonylations and deoxygenations of vancomycin reveal hydroxyl-dependent conformational effects

We have examined peptide-based catalysts for the site-selective thiocarbonylation of a protected form of vancomycin. Several catalysts were identified that either enhanced or altered the inherent selectivity profile exhibited by the substrate. Two catalysts, one identified through screening and another through rational design, were demonstrated to be effective on 0.50-g scale. Deoxygenations led ultimately to two new deoxy-vancomycin derivatives, and surprising conformational consequences of deoxygenation were revealed for one of the new compounds. These effects were mirrored in the biological activities of the new analogues and support a structural role for certain hydroxyls in the native structure.

Antibiotic activities and affinities for bacterial cell wall analogue of N-demethylvancomycin and its derivatives

N-Demethylvancomycin, which has been clinically used in China, is one member of vancomycin group (glycopeptide) antibiotics. It differs from vancomycin only in that methyl group on the amino group of the N-terminal residue of vancomycin has been replaced